Linked Life Data

2770733

Source:http://linkedlifedata.com/resource/pubmed/id/2770733

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-9-25
pubmed:abstractText
The methods of viscosimetry, the Rayleigh light-scattering and analytical ultracentrifugation were applied to study the physicochemical mechanism of the effect of fragment D on the structure of fibrin equilibrium oligomers. Using the values of intrinsic viscosity, weight average molecular masses and mass/length ratio it was shown that when producing an antipolymerization effect the fragment D retains the three-dimensional organization of fibrin polymers, i.e. rigid rod-like single- and double-stranded protofibrillas. The paper has proved that along with the traditional mechanism of inhibiting self-assembly of of the double-stranded structure due to the competition of fragment D with fibrin monomer for central domain E there is an alternative attributed to its attachment to a peripheral region of the fibrin monomer. The second mechanism is the only one which occurs in the region of single-stranded pseudoprotofibrillas existence. The role of alpha C-domains in protein-protein interactions is also discussed.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0026-8984
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
596-604
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
[Polymorphism of fibrin equilibrium oligomers in the presence of fragment D].
pubmed:publicationType
Journal Article, English Abstract